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Q09013 (DMPK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Myotonin-protein kinase

Short name=MT-PK
EC=2.7.11.1
Alternative name(s):
DM-kinase
Short name=DMK
DM1 protein kinase
DMPK
Myotonic dystrophy protein kinase
Gene names
Name:DMPK
Synonyms:DM1PK, MDPK
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length629 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Non-receptor serine/threonine protein kinase which is necessary for the maintenance of skeletal muscle structure and function. May play a role in myocyte differentiation and survival by regulating the integrity of the nuclear envelope and the expression of muscle-specific genes. May also phosphorylate PPP1R12A and inhibit the myosin phosphatase activity to regulate myosin phosphorylation. Also critical to the modulation of cardiac contractility and to the maintenance of proper cardiac conduction activity probably through the regulation of cellular calcium homeostasis. Phosphorylates PLN, a regulator of calcium pumps and may regulate sarcoplasmic reticulum calcium uptake in myocytes. May also phosphorylate FXYD1/PLM which is able to induce chloride currents. May also play a role in synaptic plasticity. Ref.12 Ref.15 Ref.16 Ref.18 Ref.21 Ref.22

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium.

Enzyme regulation

Coiled-coil-mediated oligomerization enhances the catalytic activity. Proteolytic processing of the C-terminus may release the protein from membranes and constitute a mean to regulate the enzyme. May be regulated by HSPB2, RAC1, RAF1 and G-protein second messengers. Ref.11 Ref.12 Ref.13 Ref.17

Subunit structure

Homodimer; homodimerization stimulates the kinase activity. Interacts with HSPB2; may enhance DMPK kinase activity. Interacts with PLN; phosphorylates PLN. May interact with RAC1; may regulate DMPK kinase activity. Interacts with LMNA; may regulate nuclear envelope stability. Ref.11 Ref.12 Ref.13 Ref.17 Ref.18 Ref.22 Ref.24 Ref.25

Subcellular location

Endoplasmic reticulum membrane; Single-pass type IV membrane protein; Cytoplasmic side By similarity. Nucleus outer membrane; Single-pass type IV membrane protein; Cytoplasmic side Probable. Mitochondrion outer membrane; Single-pass type IV membrane protein Probable. Sarcoplasmic reticulum membrane By similarity. Cell membrane By similarity. Cytoplasmcytosol By similarity. Note: Localizes to sarcoplasmic reticulum membranes of cardiomyocytes By similarity. Ref.12 Ref.19 Ref.22

Isoform 1: Mitochondrion membrane Ref.12 Ref.19 Ref.22.

Isoform 3: Mitochondrion membrane Ref.12 Ref.19 Ref.22.

Tissue specificity

Most isoforms are expressed in many tissues including heart, skeletal muscle, liver and brain, except for isoform 2 which is only found in the heart and skeletal muscle, and isoform 14which is only found in the brain, with high levels in the striatum, cerebellar cortex and pons. Ref.9

Domain

The coiled coil domain is required for homodimerization and regulates the enzymatic activity. Ref.23 Ref.24

Post-translational modification

Phosphorylated. Autophosphorylates. Phosphorylation by RAF1 may result in activation of DMPK. Ref.13

Proteolytic processing of the C-terminus may remove the transmembrane domain and release the kinase from membranes stimulating its activity.

Involvement in disease

Dystrophia myotonica 1 (DM1) [MIM:160900]: A muscular disorder characterized by myotonia, muscle wasting in the distal extremities, cataract, hypogonadism, defective endocrine functions, male baldness and cardiac arrhythmias.
Note: The disease is caused by mutations affecting the gene represented in this entry. The causative mutation is a CTG expansion in the 3'-UTR of the DMPK gene. A length exceeding 50 CTG repeats is pathogenic, while normal individuals have 5 to 37 repeats. Intermediate alleles with 35-49 triplets are not disease-causing but show instability in intergenerational transmissions. Disease severity varies with the number of repeats: mildly affected persons have 50 to 150 repeats, patients with classic DM have 100 to 1,000 repeats, and those with congenital onset can have more than 2,000 repeats. Ref.1 Ref.8 Ref.10 Ref.20

Sequence similarities

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. DMPK subfamily.

Contains 1 AGC-kinase C-terminal domain.

Contains 1 protein kinase domain.

Sequence caution

The sequence AAA64884.1 differs from that shown. Reason: Frameshift at positions 56, 555 and 568.

The sequence AAA87583.1 differs from that shown. Reason: Probable cloning artifact.

Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasm
Endoplasmic reticulum
Membrane
Mitochondrion
Mitochondrion outer membrane
Nucleus
Sarcoplasmic reticulum
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseCataract
   DomainCoiled coil
Transmembrane
Transmembrane helix
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular calcium ion homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

muscle cell apoptotic process

Inferred from direct assay PubMed 18729234. Source: UniProtKB

nuclear envelope organization

Inferred from mutant phenotype Ref.22. Source: UniProtKB

regulation of excitatory postsynaptic membrane potential involved in skeletal muscle contraction

Inferred from electronic annotation. Source: Ensembl

regulation of heart contraction

Inferred from direct assay Ref.18. Source: UniProtKB

regulation of myotube differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of skeletal muscle contraction by calcium ion signaling

Inferred from electronic annotation. Source: Ensembl

regulation of sodium ion transport

Inferred from electronic annotation. Source: Ensembl

regulation of synapse structural plasticity

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytosol

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of mitochondrial outer membrane

Inferred from direct assay Ref.19. Source: UniProtKB

nuclear membrane

Inferred from sequence or structural similarity. Source: UniProtKB

nuclear outer membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

sarcoplasmic reticulum membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionATP binding

Inferred from direct assay Ref.12. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

myosin phosphatase regulator activity

Inferred from direct assay Ref.16. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from direct assay Ref.12Ref.16. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PLNP266784EBI-692774,EBI-692836

Alternative products

This entry describes 12 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q09013-9)

Also known as: DMPK A;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q09013-11)

Also known as: DMPK B;

The sequence of this isoform differs from the canonical sequence as follows:
     378-382: Missing.
Isoform 3 (identifier: Q09013-16)

Also known as: DMPK C;

The sequence of this isoform differs from the canonical sequence as follows:
     550-629: LDGPPAVAVG...WRRPGAARAP → MAPRPWLWAS...AQEPPALPEP
Note: No experimental confirmation available.
Isoform 4 (identifier: Q09013-15)

Also known as: DMPK D;

The sequence of this isoform differs from the canonical sequence as follows:
     378-382: Missing.
     550-629: LDGPPAVAVG...WRRPGAARAP → MAPRPWLWAS...AQEPPALPEP
Isoform 5 (identifier: Q09013-10)

Also known as: DMPK E;

The sequence of this isoform differs from the canonical sequence as follows:
     534-535: AV → GP
     536-629: Missing.
Note: No experimental confirmation available.
Isoform 6 (identifier: Q09013-12)

Also known as: DMPK F;

The sequence of this isoform differs from the canonical sequence as follows:
     378-382: Missing.
     534-535: AV → GP
     536-629: Missing.
Note: No experimental confirmation available.
Isoform 7 (identifier: Q09013-1)

The sequence of this isoform differs from the canonical sequence as follows:
     1-53: MSAEVRLRRL...DKYVADFLQW → MGGHFWPPEP...PRFFSPTTPP
Isoform 8 (identifier: Q09013-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-89: Missing.
Note: No experimental confirmation available.
Isoform 9 (identifier: Q09013-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-53: MSAEVRLRRL...DKYVADFLQW → MGGHFWPPEP...PRFFSPTTPP
     226-275: Missing.
Note: No experimental confirmation available.
Isoform 10 (identifier: Q09013-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-53: MSAEVRLRRL...DKYVADFLQW → MGGHFWPPEP...PRFFSPTTPP
     378-382: Missing.
Note: No experimental confirmation available.
Isoform 11 (identifier: Q09013-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-53: MSAEVRLRRL...DKYVADFLQW → MGGHFWPPEP...PRFFSPTTPP
     550-579: Missing.
Note: No experimental confirmation available.
Isoform 12 (identifier: Q09013-8)

The sequence of this isoform differs from the canonical sequence as follows:
     1-53: MSAEVRLRRL...DKYVADFLQW → MGGHFWPPEP...PRFFSPTTPP
     534-535: AV → GP
     536-629: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 629629Myotonin-protein kinase
PRO_0000085924

Regions

Topological domain1 – 590590Cytoplasmic Potential
Transmembrane591 – 61121Helical; Anchor for type IV membrane protein; Potential
Topological domain612 – 62918Lumenal Potential
Domain71 – 339269Protein kinase
Domain340 – 41576AGC-kinase C-terminal
Nucleotide binding77 – 859ATP By similarity
Coiled coil457 – 53680 Ref.23 Ref.24

Sites

Active site1951Proton acceptor By similarity
Binding site1001ATP

Amino acid modifications

Modified residue2161Phosphoserine; by autocatalysis By similarity
Modified residue2281Phosphoserine; by autocatalysis By similarity
Modified residue2341Phosphothreonine; by autocatalysis By similarity

Natural variations

Alternative sequence1 – 8989Missing in isoform 8.
VSP_042098
Alternative sequence1 – 5353MSAEV…DFLQW → MGGHFWPPEPYTVFMWGSPW EADSPRVKLRGREKGRQTEG GAFPLVSSALSGDPRFFSPT TPP in isoform 7, isoform 9, isoform 10, isoform 11 and isoform 12.
VSP_042099
Alternative sequence226 – 27550Missing in isoform 9.
VSP_042100
Alternative sequence378 – 3825Missing in isoform 2, isoform 4, isoform 6 and isoform 10.
VSP_042101
Alternative sequence534 – 5352AV → GP in isoform 5, isoform 6 and isoform 12.
VSP_042102
Alternative sequence536 – 62994Missing in isoform 5, isoform 6 and isoform 12.
VSP_042103
Alternative sequence550 – 62980LDGPP…AARAP → MAPRPWLWASARWWGQAPCT AATCCSLPGSLGLAYRRRFP CSCSPLFCLVPPPWAALGWW PTPANSPQSGAAQEPPALPE P in isoform 3 and isoform 4.
VSP_042104
Alternative sequence550 – 57930Missing in isoform 11.
VSP_042105
Natural variant4231L → V. Ref.2 Ref.3 Ref.4 Ref.8
Corresponds to variant rs527221 [ dbSNP | Ensembl ].
VAR_058334
Natural variant4281L → V in a lung small cell carcinoma sample; somatic mutation. Ref.26
VAR_040452

Experimental info

Mutagenesis1001K → A: Loss of kinase activity. Ref.18
Sequence conflict4741A → P in AAB31800. Ref.5

Secondary structure

..................................................................... 629
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (DMPK A) [UniParc].

Last modified December 14, 2011. Version 3.
Checksum: 46783ED4AE65B493

FASTA62969,385
        10         20         30         40         50         60 
MSAEVRLRRL QQLVLDPGFL GLEPLLDLLL GVHQELGASE LAQDKYVADF LQWAEPIVVR 

        70         80         90        100        110        120 
LKEVRLQRDD FEILKVIGRG AFSEVAVVKM KQTGQVYAMK IMNKWDMLKR GEVSCFREER 

       130        140        150        160        170        180 
DVLVNGDRRW ITQLHFAFQD ENYLYLVMEY YVGGDLLTLL SKFGERIPAE MARFYLAEIV 

       190        200        210        220        230        240 
MAIDSVHRLG YVHRDIKPDN ILLDRCGHIR LADFGSCLKL RADGTVRSLV AVGTPDYLSP 

       250        260        270        280        290        300 
EILQAVGGGP GTGSYGPECD WWALGVFAYE MFYGQTPFYA DSTAETYGKI VHYKEHLSLP 

       310        320        330        340        350        360 
LVDEGVPEEA RDFIQRLLCP PETRLGRGGA GDFRTHPFFF GLDWDGLRDS VPPFTPDFEG 

       370        380        390        400        410        420 
ATDTCNFDLV EDGLTAMVSG GGETLSDIRE GAPLGVHLPF VGYSYSCMAL RDSEVPGPTP 

       430        440        450        460        470        480 
MELEAEQLLE PHVQAPSLEP SVSPQDETAE VAVPAAVPAA EAEAEVTLRE LQEALEEEVL 

       490        500        510        520        530        540 
TRQSLSREME AIRTDNQNFA SQLREAEARN RDLEAHVRQL QERMELLQAE GATAVTGVPS 

       550        560        570        580        590        600 
PRATDPPSHL DGPPAVAVGQ CPLVGPGPMH RRHLLLPARV PRPGLSEALS LLLFAVVLSR 

       610        620 
AAALGCIGLV AHAGQLTAVW RRPGAARAP 

« Hide

Isoform 2 (DMPK B) [UniParc].

Checksum: 7ECA31ED9A84E7E1
Show »

FASTA62469,028
Isoform 3 (DMPK C) [UniParc].

Checksum: 52B2B388CD99AA2F
Show »

FASTA63069,950
Isoform 4 (DMPK D) [UniParc].

Checksum: 10EA0187F4AD4B7C
Show »

FASTA62569,592
Isoform 5 (DMPK E) [UniParc].

Checksum: 9A08CEA02FAE8828
Show »

FASTA53559,804
Isoform 6 (DMPK F) [UniParc].

Checksum: 5E41498FDA6C22D4
Show »

FASTA53059,446
Isoform 7 [UniParc].

Checksum: 69A831604F7F8D38
Show »

FASTA63970,371
Isoform 8 [UniParc].

Checksum: A7BB715CB845055C
Show »

FASTA54059,334
Isoform 9 [UniParc].

Checksum: 2558F658CFA1FCE1
Show »

FASTA58965,076
Isoform 10 [UniParc].

Checksum: 94F39ADE9A8F4AFC
Show »

FASTA63470,014
Isoform 11 [UniParc].

Checksum: 58A97059F9590719
Show »

FASTA60967,263
Isoform 12 [UniParc].

Checksum: EF016FDBE3933553
Show »

FASTA54560,790

References

« Hide 'large scale' references
[1]"An unstable triplet repeat in a gene related to myotonic muscular dystrophy."
Fu Y.-H., Pizzuti A., Fenwick R.G. Jr., King J., Rajnarayan S., Dunne P.W., Dubel J., Nasser G.A., Ashizawa T., de Jong P.J., Wieringa B., Korneluk R., Perryman M.B., Epstein H.F., Caskey C.T.
Science 255:1256-1258(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7), INVOLVEMENT IN DM1.
[2]"Genomic organization and transcriptional units at the myotonic dystrophy locus."
Shaw D.J., McCurrach M., Rundle S.A., Harley H.G., Crow S.R., Sohn R., Thirion J.-P., Hamshere M.G., Buckler A.J., Harper P.S., Housman D.E., Brook J.D.
Genomics 18:673-679(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), VARIANT VAL-423.
Tissue: Brain and Muscle.
[3]"Structure and genomic sequence of the myotonic dystrophy (DM kinase) gene."
Mahadevan M.S., Amemiya C., Jansen G., Sabourin L., Baird S., Neville C.E., Wormskamp N., Segers B., Batzer M., Lamerdin J., de Jong P.J., Wieringa B., Korneluk R.G.
Hum. Mol. Genet. 2:299-304(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2; 5; 6), VARIANT VAL-423.
[4]"Decreased expression of myotonin-protein kinase messenger RNA and protein in adult form of myotonic dystrophy."
Fu Y.-H., Friedman D.L., Richards S., Pearlman J.A., Gibbs R.A., Pizzuti A., Ashizawa T., Perryman M.B., Scarlato G., Fenwick R.G. Jr., Caskey C.T.
Science 260:235-238(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 7; 8; 9; 10; 11 AND 12), VARIANT VAL-423.
[5]"Expression of a novel human myotonin protein kinase (MtPK) cDNA clone which encodes a protein with a thymopoietin-like domain in COS cells."
Sasagawa N., Sorimachi H., Maruyama K., Arahata K., Ishiura S., Suzuki K.
FEBS Lett. 351:22-26(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
Tissue: Muscle.
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Prostate.
[8]"Molecular basis of myotonic dystrophy: expansion of a trinucleotide (CTG) repeat at the 3' end of a transcript encoding a protein kinase family member."
Brook J.D., McCurrach M., Harley H.G., Buckler A.J., Church D., Aburatani H., Hunter K., Stanton V.P., Thirion J.-P., Hudson T., Sohn R., Zemelman B., Snell R.G., Rundle S.A., Crow S., Davies J., Shelbourne P., Buxton J. expand/collapse author list , Jones C., Juvonen V., Johnson K., Harper P.S., Shaw D.J., Housman D.E.
Cell 68:799-808(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 43-629 (ISOFORM 2), INVOLVEMENT IN DM1, VARIANT VAL-423.
[9]"Different expression of the myotonin protein kinase gene in discrete areas of human brain."
Gennarelli M., Lucarelli M., Zelano G., Pizzuti A., Novelli G., Dallapiccola B.
Biochem. Biophys. Res. Commun. 216:489-494(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 550-619 (ISOFORM 1), TISSUE SPECIFICITY.
Tissue: Brain.
[10]"Characterization of the myotonic dystrophy region predicts multiple protein isoform-encoding mRNAs."
Jansen G., Mahadevan M.S., Amemiya C., Wormskamp N., Segers B., Hendriks W., O'Hoy K., Baird S., Sabourin L., Lennon G., Jap P.L., Iles D., Coerwinkel M., Hofker M., Carrano A.V., de Jong P.J., Korneluk R.G., Wieringa B.
Nat. Genet. 1:261-266(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING, INVOLVEMENT IN DM1.
Tissue: Brain and Heart.
[11]"MKBP, a novel member of the small heat shock protein family, binds and activates the myotonic dystrophy protein kinase."
Suzuki A., Sugiyama Y., Hayashi Y., Nyu-i N., Yoshida M., Nonaka I., Ishiura S., Arahata K., Ohno S.
J. Cell Biol. 140:1113-1124(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HSPB2, ENZYME REGULATION.
Tissue: Muscle.
[12]"Myotonic dystrophy protein kinase domains mediate localization, oligomerization, novel catalytic activity, and autoinhibition."
Bush E.W., Helmke S.M., Birnbaum R.A., Perryman M.B.
Biochemistry 39:8480-8490(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION, HOMODIMERIZATION, SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING.
[13]"Rac-1 and Raf-1 kinases, components of distinct signaling pathways, activate myotonic dystrophy protein kinase."
Shimizu M., Wang W., Walch E.T., Dunne P.W., Epstein H.F.
FEBS Lett. 475:273-277(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAC1, PHOSPHORYLATION BY RAF1, ENZYME REGULATION.
[14]"Constitutive and regulated modes of splicing produce six major myotonic dystrophy protein kinase (DMPK) isoforms with distinct properties."
Groenen P.J.T.A., Wansink D.G., Coerwinkel M., van den Broek W., Jansen G., Wieringa B.
Hum. Mol. Genet. 9:605-616(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3; 4; 5 AND 6).
[15]"Phospholemman is a substrate for myotonic dystrophy protein kinase."
Mounsey J.P., John J.E. III, Helmke S.M., Bush E.W., Gilbert J., Roses A.D., Perryman M.B., Jones L.R., Moorman J.R.
J. Biol. Chem. 275:23362-23367(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF FXYD1/PLM.
[16]"Myotonic dystrophy protein kinase phosphorylates the myosin phosphatase targeting subunit and inhibits myosin phosphatase activity."
Muranyi A., Zhang R., Liu F., Hirano K., Ito M., Epstein H.F., Hartshorne D.J.
FEBS Lett. 493:80-84(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF PPP1R12A.
[17]"Homodimerization through coiled-coil regions enhances activity of the myotonic dystrophy protein kinase."
Zhang R., Epstein H.F.
FEBS Lett. 546:281-287(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: HOMODIMERIZATION, ENZYME REGULATION.
[18]"Myotonic dystrophy protein kinase phosphorylates phospholamban and regulates calcium uptake in cardiomyocyte sarcoplasmic reticulum."
Kaliman P., Catalucci D., Lam J.T., Kondo R., Gutierrez J.C., Reddy S., Palacin M., Zorzano A., Chien K.R., Ruiz-Lozano P.
J. Biol. Chem. 280:8016-8021(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF PLN, MUTAGENESIS OF LYS-100, INTERACTION WITH PLN.
[19]"Divergent mitochondrial and endoplasmic reticulum association of DMPK splice isoforms depends on unique sequence arrangements in tail anchors."
van Herpen R.E., Oude Ophuis R.J., Wijers M., Bennink M.B., van de Loo F.A., Fransen J., Wieringa B., Wansink D.G.
Mol. Cell. Biol. 25:1402-1414(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING, SUBCELLULAR LOCATION.
[20]"Highly unstable sequence interruptions of the CTG repeat in the myotonic dystrophy gene."
Musova Z., Mazanec R., Krepelova A., Ehler E., Vales J., Jaklova R., Prochazka T., Koukal P., Marikova T., Kraus J., Havlovicova M., Sedlacek Z.
Am. J. Med. Genet. A 149:1365-1374(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN DM1.
[21]"Chelerythrine perturbs lamellar actomyosin filaments by selective inhibition of myotonic dystrophy kinase-related Cdc42-binding kinase."
Tan I., Lai J., Yong J., Li S.F., Leung T.
FEBS Lett. 585:1260-1268(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF PPP1R12A.
[22]"Myotonic dystrophy protein kinase is critical for nuclear envelope integrity."
Harmon E.B., Harmon M.L., Larsen T.D., Yang J., Glasford J.W., Perryman M.B.
J. Biol. Chem. 286:40296-40306(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN NUCLEAR ENVELOPE STABILITY, SUBCELLULAR LOCATION, INTERACTION WITH LMNA.
[23]"Crystallization and preliminary X-ray analysis of the coiled-coil domain of dystrophia myotonica kinase."
Garcia P., Marino M., Mayans O.
Acta Crystallogr. D 60:2336-2339(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 460-537, COILED-COIL DOMAIN.
[24]"Molecular insights into the self-assembly mechanism of dystrophia myotonica kinase."
Garcia P., Ucurum Z., Bucher R., Svergun D.I., Huber T., Lustig A., Konarev P.V., Marino M., Mayans O.
FASEB J. 20:1142-1151(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 460-537, SUBUNIT, COILED-COIL DOMAIN.
[25]"Structure of dystrophia myotonica protein kinase."
Elkins J.M., Amos A., Niesen F.H., Pike A.C.W., Fedorov O., Knapp S.
Protein Sci. 18:782-791(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 11-430 IN COMPLEX WITH INHIBITOR BIM-8, SUBUNIT.
[26]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-428.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M87312 mRNA. No translation available.
L19268 mRNA. Translation: AAA36206.1.
L19266 Genomic DNA. Translation: AAA36205.1.
L08835 Genomic DNA. Translation: AAC14449.1.
L08835 Genomic DNA. Translation: AAC14451.1.
L08835 Genomic DNA. Translation: AAC14448.1.
L08835 Genomic DNA. Translation: AAC14450.1.
L00727 Genomic DNA. Translation: AAA75235.1.
L00727 Genomic DNA. Translation: AAA75236.1.
L00727 Genomic DNA. Translation: AAA75237.1.
L00727 Genomic DNA. Translation: AAA75238.1.
L00727 Genomic DNA. Translation: AAA75239.1.
L00727 Genomic DNA. Translation: AAA75240.1.
S72883 mRNA. Translation: AAB31800.1.
CH471126 Genomic DNA. Translation: EAW57382.1.
BC062553 mRNA. Translation: AAH62553.1.
M94203 mRNA. Translation: AAA64884.1. Frameshift.
U46546 mRNA. Translation: AAA87583.1. Sequence problems.
PIRB49364.
RefSeqNP_001075029.1. NM_001081560.2.
NP_001075031.1. NM_001081562.2.
NP_001075032.1. NM_001081563.2.
NP_001275694.1. NM_001288765.1.
NP_004400.4. NM_004409.4.
UniGeneHs.631596.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WT6X-ray1.60A/B/D460-537[»]
2VD5X-ray2.80A/B11-420[»]
ProteinModelPortalQ09013.
SMRQ09013. Positions 11-416, 461-527.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108100. 14 interactions.
IntActQ09013. 15 interactions.
MINTMINT-195910.
STRING9606.ENSP00000345997.

Chemistry

BindingDBQ09013.
ChEMBLCHEMBL5320.
GuidetoPHARMACOLOGY1505.

PTM databases

PhosphoSiteQ09013.

Polymorphism databases

DMDM254763287.

2D gel databases

REPRODUCTION-2DPAGEQ09013.

Proteomic databases

PaxDbQ09013.
PRIDEQ09013.

Protocols and materials databases

DNASU1760.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000291270; ENSP00000291270; ENSG00000104936. [Q09013-9]
ENST00000343373; ENSP00000345997; ENSG00000104936. [Q09013-1]
ENST00000354227; ENSP00000346168; ENSG00000104936. [Q09013-12]
ENST00000447742; ENSP00000413417; ENSG00000104936. [Q09013-11]
ENST00000458663; ENSP00000401753; ENSG00000104936. [Q09013-15]
GeneID1760.
KEGGhsa:1760.
UCSCuc002pdf.1. human. [Q09013-9]
uc010xxs.1. human. [Q09013-16]
uc010xxt.1. human. [Q09013-12]

Organism-specific databases

CTD1760.
GeneCardsGC19M046272.
H-InvDBHIX0137522.
HGNCHGNC:2933. DMPK.
HPAHPA007164.
HPA008905.
MIM160900. phenotype.
605377. gene.
neXtProtNX_Q09013.
Orphanet273. Steinert myotonic dystrophy.
PharmGKBPA27380.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233033.
HOVERGENHBG107817.
KOK08788.
OMATLSDMQE.
OrthoDBEOG7F511X.
TreeFamTF105337.

Enzyme and pathway databases

BRENDA2.7.11.1. 2681.
SignaLinkQ09013.

Gene expression databases

ArrayExpressQ09013.
BgeeQ09013.
CleanExHS_DMPK.
GenevestigatorQ09013.

Family and domain databases

InterProIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR014930. Myotonic_dystrophy_kinase_coil.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF08826. DMPK_coil. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
ProDomPD011252. Myotonic_dystrophy_kinase_coil. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDMPK. human.
EvolutionaryTraceQ09013.
GeneWikiMyotonin-protein_kinase.
GenomeRNAi1760.
NextBio7169.
PROQ09013.
SOURCESearch...

Entry information

Entry nameDMPK_HUMAN
AccessionPrimary (citable) accession number: Q09013
Secondary accession number(s): Q16205, Q6P5Z6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: December 14, 2011
Last modified: March 19, 2014
This is version 149 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM